Abstract
6-β-(Trifluoromethane sulfonyl)-amido-penicillanic acid sulfone was found to be a potent inhibitor ofBacillus licheniformis 749/C β-lactamase. Rates of inactivation of the enzyme by this inhibitor increased with decreasingpH of the reaction medium. The irreversible inactivation of the enzyme was accompanied by a stoichiometric incorporation of I mole of the inhibitor per mole of protein, resulting in the appearance of a chromophore (λmax, 310 nm). Analysis of the chromophoric peptide isolated from the tryptic digest of the inactivated protein revealed the presence of the label in the segment corresponding to residues 66–73 in the primary structure of the enzyme.
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Hilhorst, I.M., Dmitrienko, G.I., Viswanatha, T. et al. Bacillus licheniformis 749/C β-lactamase inactivated by 6-β-(Trifluoromethane sulfonyl)-amido-penicillanic acid sulfone. J Protein Chem 3, 275–286 (1984). https://doi.org/10.1007/BF01034895
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DOI: https://doi.org/10.1007/BF01034895